Recombinant Human IL-1 RII Fc Chimera Protein, CF

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human IL-1 RII Fc Chimera Protein, CF Summary

• Details of Functionality: Measured by its ability to inhibit IL-1 beta -dependent proliferation in D10.G4.1 mouse helper T cells. Symons, J.A. et al. (1987) in Lymphokines and Interferons, a Practical Approach. Clemens, M.J. et al. (eds): IRL Press. 272.

  Approximately 0.3-1.8 μg/mL of Recombinant Human (rh) IL‑1 RII Fc Chimera will inhibit 50% of the biological response due to 50 pg/mL of rhIL-1 beta .

• Source: Chinese Hamster Ovary cell line, CHO-derived human IL-1 RII protein
  

  Human IL-1 RII (His21 - Glu343) Accession # P27930	IEGRMD	Human IgG1 (Pro100 - Lys330)
  N-terminus		C-terminus

• Accession #: P27930
• N-terminal Sequence: His21
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Gene: IL1R2
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
• Endotoxin Note: <0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 63.7 kDa (monomer).
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
• SDS-PAGE: 80-95 kDa, reducing conditions

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS.
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
• Reconstitution Instructions: Reconstitute at 100 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human IL-1 RII Fc Chimera Protein, CF

• beta
• CD121b antigen
• CD121b
• IL-1 R beta
• IL-1 RII
• IL1R2
• IL1RBCD121 antigen-like family member B
• IL-1R-beta
• IL1RII
• IL-1RII
• IL-1RT2
• IL-1RT-2
• interleukin 1 receptor, type II
• Interleukin-1 receptor beta
• MGC47725

Background

IL-1 Receptor II (also IL‑1 R2) is a 60 ‑ 70 kDa member of the interleukin‑1 receptor family of proteins (1 ‑ 4). It serves as a non‑signaling ligand‑binding decoy receptor for IL‑1 beta and IL‑1 alpha  (4). IL‑1 binds to a cell surface complex composed of IL‑1 RI and IL‑1 RAcP. Upon activation, this complex recruits MyD88 for downstream signaling (4, 5). The proinflammatory action of IL-1 is antagonized by IL‑1ra which binds to IL‑1 RI but does not initiate signaling. A second natural antagonist is IL‑1 RII, a cell surface receptor that binds both IL‑1 alpha and beta , but not IL‑1ra. IL‑1 RII is found on astrocytes, neutrophils, anterior pituitary acidophils that secrete GH, corneal epithelium, testicular Leydig and Sertoli cells, B cells and monocytes/macrophages (6 ‑ 12). Mature human IL‑1 RII is a 385 amino acid (aa) type I transmembrane glycoprotein that contains a 330 aa extracellular region with three Ig‑like domains (aa 14 ‑ 343), a 26 aa transmembrane segment, and a 29 aa cytoplasmic domain with no signaling motifs (13). There is one soluble 55 ‑ 60 kDa alternative splice form that shows a premature truncation after Gln296 (14). ARTS‑1 mediated cleavage of IL-1 RII generates a 47 kDa isoform, while alpha ‑secretase cleavage after Arg338 creates a 50 ‑ 55 kDa isoform that undergoes further processing back to Pro314 (15, 16). Human IL‑1 RII shares 59% aa identity with mouse IL‑1 RII in the extracellular region. Different forms of human IL‑1 RII demonstrate differing binding affinities for IL‑1. IL‑1 RII has a preference for IL‑1 beta over IL‑1 alpha , and binding requires the presence of IL‑1 RAcP. This interaction prevents the association of IL‑1 with IL‑1 RI and also restricts IL‑1 R to a non‑signaling receptor complex (11, 17 ‑ 19). The membrane IL‑1 RII:IL‑1 RAcP complex does not form a functional bond with IL‑1ra, and cannot bind pro‑IL‑1 beta (11, 13, 19, 20). Soluble IL‑1 RII, by contrast, demonstrates a different binding profile. Notably, it will bind pro‑IL‑1 beta rendering it unavailable for activation by extracellular proteases (19, 20). Although it will sequester both IL‑1 beta and IL‑1 alpha , its interaction with soluble IL‑1 RAcP creates a circulating high affinity complex for both IL‑1 beta and IL‑1 alpha , thus potentiating its anti‑inflammatory activity.

1. Dinarello, C.A. (2011) Blood 117:3720.
2. Boraschi, D. and A. Tagliabue (2006) Vitam. Horm. 74:229.
3. Dunne, A. and L.A.J. O’Neill (2003) Sci STKE. Feb 25;2003(171):re3.
4. Dinarello, C.A. (2009) Annu. Rev. Immunol. 27:519.
5. O’Neill, L.A.J. (2008) Immunol. Rev. 226:10.
6. Pousset, F. et al. (2001) J. Neurochem. 79:726.
7. Bourke, E. et al. (2003) J. Immunol. 170:5999.
8. French, R.A. et al. (1996) Endocrinology 137:4027.
9. Cubitt, C.L. et al. (2001) Invest. Ophthalmol. Vis. Sci. 42:701.
10. Gomez, E. et al. (1997) Biol. Reprod. 56:1513.
11. Lang, D. et al. (1998) J. Immunol. 161:6871.
12. Mantovani, A. et al. (2001) Trends Immunol. 22:328.
13. McMahan, C.J. et al. (1991) EMBO J. 10:2821.
14. Liu, C. et al. (1996) J. Biol. Chem. 271:20965.
15. Cui, X. et al. (2003) J. Immunol. 171:6814.
16. Kuhn, P-H. et al. (2007) J. Biol. Chem. 282:11982.
17. Smith, D.E. et al. (2003) Immunity 18:87.
18. Makinowsky, D. et al. (1998) FEBS Lett. 429:299.
19. Neumann, D. et al. (2000) J. Immunol. 165:3350.
20. Symons, J. A. et al. (1995) Proc. Natl. Acad. Sci. USA 92:1714.
21. Wang, D. et al. (2010) Nat. Immunol. 11:905.

Bioinformatics

• Gene Symbol: IL1R2
• Uniprot:
  • P27930()